Evidence map›Paper›PMID 40691738›Full record

ReviewApoptosis : an international journal on programmed cell death2025

Disrupting membranes, controlling cell fate: the role of pore-forming proteins in cell death and therapy.

Sonia Iranpour, Maryam Arif, Eva Szegezdi

Abstract readReview
In one paragraph

Review in Apoptosis : an international journal on programmed cell death, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Sonia IranpourSchool of Biological and Chemical Sciences, University of Galway, Galway, Ireland.
Maryam ArifSchool of Biological and Chemical Sciences, University of Galway, Galway, Ireland.
Eva SzegezdiSchool of Biological and Chemical Sciences, University of Galway, Galway, Ireland. eva.szegezdi@universityofgalway.ie.ORCID 0000-0002-5708-3535

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pore-forming proteins (PFPs), characterized by their ability to form pores or disrupt membranes are now recognized as key executioners of cell death, either as effectors of the immune system (non-cell-autonomous function), or of regulated cell death programs (cell autonomous function). To perforate membranes, most PFPs transition from water-soluble monomers or oligomers into multimeric and often supramolecular complexes, a process achieved via substantial structural transition of the PFP. Although they share the general ability to perforate cellular or intracellular membranes, PFPs differ in their membrane-binding preferences, the structural and functional characteristics of the pores they form (such as pore size, pore structure and ability to trigger membrane rupture) and the cell death mechanism they induce or execute. Herein, we review the specific traits of all key human PFPs, including their membrane specificity, regulation of their activity and the structure of the membrane pores they form, followed by insights into the therapeutic potential of PFPs and harnessing their abilities for cancer therapy.

Indexed as

ApoptosisCell DeathCell MembraneNeoplasmsPore Forming Cytotoxic ProteinsAnimalsHumansPore Forming Cytotoxic ProteinsCancer therapyGasderminGranulysinMixed lineage kinase domain-like pseudokinase (MLKL)Ninjurin-1PerforinPore-forming proteins (PFP)Regulated cell death

Identifiers

PMID40691738
PMCPMC12474679

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.